A purified alkaline thermo-tolerant bacterial lipase from Bacillus cereus MTCC 8372 was immobilized on a Poly (MAc-co-DMA-cl-MBAm) hydrogel. The hydrogel showed approximately 94% binding capacity for lipase. The immobilized lipase (2.36 IU) was used to achieve esterification ofmyristic acid and isopropanol in n-heptane at 65 degrees C under continuous shaking. The myristic acid and isopropanol when used at a concentration of 100 mM each in n-heptane resulted in formation of isopropyl myristate (66.0 +/- 0.3 mM) in 15 h. The reaction temperature below or higher than 65 degrees C markedly reduced the formation of isopropyl myristate. Addition of a molecular sieve (3 A x 1.5 mm) to the reaction mixture drastically reduced the ester formation. The hydrogel bound lipase when repetitively used to perform esterification under optimized conditions resulted in 38.0 +/- 0.2 mM isopropyl myristate after the 3rd cycle of esterification.